|Entry||Database: EMDB / ID: 3577|
|Source||Homo sapiens / / human|
|Method||single particle reconstruction / 38 Å resolution|
|Authors||Brasen C / Dorosz J / Wiuf A / Boesen T / Mirza O / Gajhede M|
|Citation||Journal: Biochim. Biophys. Acta / Year: 2017|
Title: Expression, purification and characterization of the human MTA2-RBBP7 complex.
Authors: Christoffer Brasen / Jerzy Dorosz / Anders Wiuf / Thomas Boesen / Osman Mirza / Michael Gajhede
Abstract: The repressive Nucleosome Remodeling and histone Deacetylation (NuRD) complex remodels the chromatin structure by coupling ATP-dependent remodeling activity with histone deacetylase function and ...The repressive Nucleosome Remodeling and histone Deacetylation (NuRD) complex remodels the chromatin structure by coupling ATP-dependent remodeling activity with histone deacetylase function and plays important roles in regulating gene transcription, DNA damage repair and chromatin assembly. The complex is composed of six subunits: Metastasis Associated proteins MTA1/2/3 initially recruit histone chaperones RBBP4/7 followed by the histone deacetylases HDAC1/2 forming a core complex. Further association of the CpG-binding protein MBD2/3, p66α/β and the ATP-dependent helicase CDH3/4 constitutes the NuRD complex. Recent structural studies on truncated human proteins or orthologous have revealed that the stoichiometry of the MTA1-RBBP4 complex is 2:4. This study reports expression and purification of the intact human MTA2-RBBP7 complex using HEK293F cells as expression system. In analogy with findings on the Drosophila NuRD complex, we find that also the human MTA-RBBP can be isolated in vitro. Taken together with previous findings this suggests, that MTA-RBBP is a stable complex, with a central role in the initial assembly of the human NuRD complex. Refined 3D volumes of the complex generated from negative stain electron microscopy (EM) data reveals an elongated architecture that is capable of hinge like motion around the center of the particle.
Copyright: 2017 Elsevier B.V. All rights reserved.
|Date||Deposition: Jan 17, 2017 / Header (metadata) release: Feb 15, 2017 / Map release: May 3, 2017 / Last update: May 3, 2017|
Downloads & links
|File||emd_3577.map.gz (map file in CCP4 format, 19653 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 3.15 Å|
CCP4 map header:
-Entire MTA2-RBBP7 complex
|Entire||Name: MTA2-RBBP7 complex / Number of components: 1|
-Component #1: protein, MTA2-RBBP7 complex
|Specimen||Specimen state: particle|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
Model: Tecnai Spirit / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI SPIRIT|
|Electron gun||Electron source: LAB6 / Accelerating voltage: 120 kV / Electron dose: 10 e/Å2 / Illumination mode: OTHER|
|Lens||Cs: 2.2 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: TVIPS TEMCAM-F416 (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 1267|
|3D reconstruction||Resolution: 38 Å / Resolution method: FSC 0.143 CUT-OFF|
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